histone acetyltransferase
Intramolecular
Cysteine 1702 and cysteine 1727
Cysteine 1715 and cysteine 1718
Cysteine 1702 and cysteine 1705
Cysteine 1281 and cysteine 1306
Cysteine 1702 and cysteine 1724
Cysteine 1724 and cysteine 1727
Cysteine 1303 and cysteine 1306
Cysteine 1278 and cysteine 1281
Cysteine 1278 and cysteine 1306
Cysteine 1705 and cysteine 1724
More...Cysteine 1281 and cysteine 1303
Cysteine 1705 and cysteine 1727
Cysteine 1278 and cysteine 1303
Cysteine 1194 and cysteine 1289
Cysteine 1194 and cysteine 1195
Cysteine 1195 and cysteine 1289
5u7g A 1708 A 1733
A redox-regulated disulphide may form within histone acetyltransferase between cysteines 1702 and 1727 (1708 and 1733 respectively in this structure).
Details
Redox score ?
90
PDB code
5u7g
Structure name
crystal structure of the catalytic core of cbp
Structure deposition date
2016-12-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
5
% buried
6
Peptide accession
Q8QZV8
Residue number A
1702
Residue number B
1727
Peptide name
histone acetyltransferase
Ligandability
Cysteine 1702 of histone acetyltransferase
Cysteine 1727 of histone acetyltransferase
5u7g A 1721 A 1724
A redox-regulated disulphide may form within histone acetyltransferase between cysteines 1715 and 1718 (1721 and 1724 respectively in this structure).
Details
Redox score ?
90
PDB code
5u7g
Structure name
crystal structure of the catalytic core of cbp
Structure deposition date
2016-12-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
6
% buried
0
Peptide accession
Q8QZV8
Residue number A
1715
Residue number B
1718
Peptide name
histone acetyltransferase
Ligandability
Cysteine 1715 of histone acetyltransferase
Cysteine 1718 of histone acetyltransferase
5u7g A 1708 A 1711
A redox-regulated disulphide may form within histone acetyltransferase between cysteines 1702 and 1705 (1708 and 1711 respectively in this structure).
Details
Redox score ?
88
PDB code
5u7g
Structure name
crystal structure of the catalytic core of cbp
Structure deposition date
2016-12-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
5
% buried
6
Peptide accession
Q8QZV8
Residue number A
1702
Residue number B
1705
Peptide name
histone acetyltransferase
Ligandability
Cysteine 1702 of histone acetyltransferase
Cysteine 1705 of histone acetyltransferase
5u7g B 1287 B 1312
A redox-regulated disulphide may form within histone acetyltransferase between cysteines 1281 and 1306 (1287 and 1312 respectively in this structure).
Details
Redox score ?
84
PDB code
5u7g
Structure name
crystal structure of the catalytic core of cbp
Structure deposition date
2016-12-12
Thiol separation (Å)
3
Half-sphere exposure sum ?
50
Minimum pKa ?
8
% buried
16
Peptide accession
Q8QZV8
Residue number A
1281
Residue number B
1306
Peptide name
histone acetyltransferase
Ligandability
Cysteine 1281 of histone acetyltransferase
Cysteine 1306 of histone acetyltransferase
5u7g A 1708 A 1730
A redox-regulated disulphide may form within histone acetyltransferase between cysteines 1702 and 1724 (1708 and 1730 respectively in this structure).
Details
Redox score ?
84
PDB code
5u7g
Structure name
crystal structure of the catalytic core of cbp
Structure deposition date
2016-12-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
5
% buried
8
Peptide accession
Q8QZV8
Residue number A
1702
Residue number B
1724
Peptide name
histone acetyltransferase
Ligandability
Cysteine 1702 of histone acetyltransferase
Cysteine 1724 of histone acetyltransferase
5u7g B 1730 B 1733
A redox-regulated disulphide may form within histone acetyltransferase between cysteines 1724 and 1727 (1730 and 1733 respectively in this structure).
Details
Redox score ?
83
PDB code
5u7g
Structure name
crystal structure of the catalytic core of cbp
Structure deposition date
2016-12-12
Thiol separation (Å)
3
Half-sphere exposure sum ?
55
Minimum pKa ?
8
% buried
1
Peptide accession
Q8QZV8
Residue number A
1724
Residue number B
1727
Peptide name
histone acetyltransferase
Ligandability
Cysteine 1724 of histone acetyltransferase
Cysteine 1727 of histone acetyltransferase
5u7g B 1309 B 1312
A redox-regulated disulphide may form within histone acetyltransferase between cysteines 1303 and 1306 (1309 and 1312 respectively in this structure).
Details
Redox score ?
83
PDB code
5u7g
Structure name
crystal structure of the catalytic core of cbp
Structure deposition date
2016-12-12
Thiol separation (Å)
3
Half-sphere exposure sum ?
56
Minimum pKa ?
8
% buried
18
Peptide accession
Q8QZV8
Residue number A
1303
Residue number B
1306
Peptide name
histone acetyltransferase
Ligandability
Cysteine 1303 of histone acetyltransferase
Cysteine 1306 of histone acetyltransferase
5u7g B 1284 B 1287
A redox-regulated disulphide may form within histone acetyltransferase between cysteines 1278 and 1281 (1284 and 1287 respectively in this structure).
Details
Redox score ?
81
PDB code
5u7g
Structure name
crystal structure of the catalytic core of cbp
Structure deposition date
2016-12-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
8
% buried
31
Peptide accession
Q8QZV8
Residue number A
1278
Residue number B
1281
Peptide name
histone acetyltransferase
Ligandability
Cysteine 1278 of histone acetyltransferase
Cysteine 1281 of histone acetyltransferase
5u7g A 1284 A 1312
A redox-regulated disulphide may form within histone acetyltransferase between cysteines 1278 and 1306 (1284 and 1312 respectively in this structure).
Details
Redox score ?
80
PDB code
5u7g
Structure name
crystal structure of the catalytic core of cbp
Structure deposition date
2016-12-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
8
% buried
23
Peptide accession
Q8QZV8
Residue number A
1278
Residue number B
1306
Peptide name
histone acetyltransferase
Ligandability
Cysteine 1278 of histone acetyltransferase
Cysteine 1306 of histone acetyltransferase
5u7g A 1711 A 1730
A redox-regulated disulphide may form within histone acetyltransferase between cysteines 1705 and 1724 (1711 and 1730 respectively in this structure).
Details
Redox score ?
79
PDB code
5u7g
Structure name
crystal structure of the catalytic core of cbp
Structure deposition date
2016-12-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
8
% buried
2
Peptide accession
Q8QZV8
Residue number A
1705
Residue number B
1724
Peptide name
histone acetyltransferase
Ligandability
Cysteine 1705 of histone acetyltransferase
Cysteine 1724 of histone acetyltransferase
5u7g B 1287 B 1309
A redox-regulated disulphide may form within histone acetyltransferase between cysteines 1281 and 1303 (1287 and 1309 respectively in this structure).
Details
Redox score ?
78
PDB code
5u7g
Structure name
crystal structure of the catalytic core of cbp
Structure deposition date
2016-12-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
8
% buried
28
Peptide accession
Q8QZV8
Residue number A
1281
Residue number B
1303
Peptide name
histone acetyltransferase
Ligandability
Cysteine 1281 of histone acetyltransferase
Cysteine 1303 of histone acetyltransferase
5u7g B 1711 B 1733
A redox-regulated disulphide may form within histone acetyltransferase between cysteines 1705 and 1727 (1711 and 1733 respectively in this structure).
Details
Redox score ?
77
PDB code
5u7g
Structure name
crystal structure of the catalytic core of cbp
Structure deposition date
2016-12-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
9
% buried
0
Peptide accession
Q8QZV8
Residue number A
1705
Residue number B
1727
Peptide name
histone acetyltransferase
Ligandability
Cysteine 1705 of histone acetyltransferase
Cysteine 1727 of histone acetyltransferase
5u7g A 1284 A 1309
A redox-regulated disulphide may form within histone acetyltransferase between cysteines 1278 and 1303 (1284 and 1309 respectively in this structure).
Details
Redox score ?
76
PDB code
5u7g
Structure name
crystal structure of the catalytic core of cbp
Structure deposition date
2016-12-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
8
% buried
38
Peptide accession
Q8QZV8
Residue number A
1278
Residue number B
1303
Peptide name
histone acetyltransferase
Ligandability
Cysteine 1278 of histone acetyltransferase
Cysteine 1303 of histone acetyltransferase
5u7g A 1200 A 1295
A redox-regulated disulphide may form within histone acetyltransferase between cysteines 1194 and 1289 (1200 and 1295 respectively in this structure).
Details
Redox score ?
70
PDB code
5u7g
Structure name
crystal structure of the catalytic core of cbp
Structure deposition date
2016-12-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
nan
Peptide accession
Q8QZV8
Residue number A
1194
Residue number B
1289
Peptide name
histone acetyltransferase
Ligandability
Cysteine 1194 of histone acetyltransferase
Cysteine 1289 of histone acetyltransferase
5u7g B 1200 B 1201
A redox-regulated disulphide may form within histone acetyltransferase between cysteines 1194 and 1195 (1200 and 1201 respectively in this structure).
Details
Redox score ?
68
PDB code
5u7g
Structure name
crystal structure of the catalytic core of cbp
Structure deposition date
2016-12-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
78
Peptide accession
Q8QZV8
Residue number A
1194
Residue number B
1195
Peptide name
histone acetyltransferase
Ligandability
Cysteine 1194 of histone acetyltransferase
Cysteine 1195 of histone acetyltransferase
5u7g A 1201 A 1295
A redox-regulated disulphide may form within histone acetyltransferase between cysteines 1195 and 1289 (1201 and 1295 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
5u7g
Structure name
crystal structure of the catalytic core of cbp
Structure deposition date
2016-12-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
18
% buried
nan
Peptide accession
Q8QZV8
Residue number A
1195
Residue number B
1289
Peptide name
histone acetyltransferase
Ligandability
Cysteine 1195 of histone acetyltransferase
Cysteine 1289 of histone acetyltransferase
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